Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Biochemistry & Molecular Biology Notes
Detection of Hydrolytic Activity of Trypsin with a Fluorescence-chymotryptic Peptide on a TLC Plate
Tetsuya UCHIKOBAShigeko FUKUMOTOTakao ITAKURAMichiko OKUBOKazuhiko TOMOKIYOKazunari ARIMAHiroo YONEZAWA
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2004 Volume 68 Issue 1 Pages 222-225

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Abstract
  To find a new trypsin-like enzyme, a simple assay method of the hydrolysis activity for trypsin has been found. We used 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate (AQC) in the peptide labeling as a substrate for the trypsin-like peptidase in this study. The peptidase activity of trypsin was detected by using an AQC-chymotryptic peptide (AHP1) obtained from bovine hemoglobin. This showed that the substrate specificity of trypsin-like peptidase was distinguishable from that of the others by this procedure, and the method was used extensively in cases of various trypsin inhibitors with no significant interference from the concomitant.
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© 2004 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
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